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Originally published In Press as doi:10.1074/jbc.M004678200 on September 19, 2000

J. Biol. Chem., Vol. 275, Issue 49, 38275-38280, December 8, 2000
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The TonE/TonEBP Pathway Mediates Tonicity-responsive Regulation of UT-A Urea Transporter Expression*

Yushi NakayamaDagger §, Tao Peng, Jeff M. SandsDagger , and Serena M. Bagnasco||

From the Dagger  Renal Division, Department of Medicine and the  Department of Pathology, Emory University School of Medicine, Atlanta, Georgia 30322

The rat renal urea transporter UT-A includes four isoforms. UT-A1, UT-A3, and UT-A4 are transcribed from a single initiation site at the 5'-end of the gene; a distinct internal initiation site is used for UT-A2 transcription. We cloned 1.3 kilobases (kb) of the 5'-flanking region upstream of the transcription start site of UT-A1, UT-A3, and UT-A4. This region contains three CCAAT sequences but lacks a TATA motif. A tonicity-responsive enhancer (TonE) was identified at -377bp. The 1.3-kb full fragment subcloned into pGL3 vector induced luciferase activity in Madin-Darby canine kidney cells and in mouse inner medullary collecting duct cells in isotonic medium. Luciferase activity was increased significantly in hypertonic medium, whereas deletion or mutation of the TonE sequence abolished this response. Electrophoretic mobility shift assay using the 5' UT-A TonE sequence as DNA probe showed formation of a specific DNA-protein complex with nuclear extracts from cells exposed to hypertonic medium and was weakly detectable in isotonic controls. A supershift in the mobility of the DNA-protein complex was observed with antiserum targeted to the TonE-binding protein (TonEBP). Co-transfection with dominant-negative TonEBP abolished the luciferase activity induced by the UT-A 1.3-kb construct under hypertonic and isotonic conditions. These data suggest that the TonE/TonEBP pathway mediates tonicity-responsive transcriptional regulation of UT-A1, UT-A3, and UT-A4 expression.

* This work was supported in part by National Institutes of Health Grants P01-DK50268, R01-DK41707, R01-DK53917, and Grant-in aid 96006090 from the American Heart Association. Part of this work was presented at the Experimental Biology Meeting, April 15-18, 2000 in San Diego, CA (Nakayama, Y., Peng, T., Sands, J. M., and Bagnasco, S. M. (2000) FASEB J. 14, A348 (abstr.)).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF214483.

§ Supported by a fellowship from the National Kidney Foundation of Georgia.

|| To whom correspondence should be addressed: Dept. of Pathology, Emory University School of Medicine, WMB Rm. 7105 A, 1639 Pierce Dr., NE, Atlanta, GA 30322. Tel.: 404-727-4026; Fax: 404-727-8540; E-mail: sbagnas@emory.edu.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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